1kok

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kok.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kok.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kok| PDB=1kok | SCENE= }}
{{STRUCTURE_1kok| PDB=1kok | SCENE= }}
-
'''Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)'''
+
===Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)===
-
==Overview==
+
<!--
-
The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12237229}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12237229 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12237229}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Proximal loop]]
[[Category: Proximal loop]]
[[Category: Trp191 cationic radical]]
[[Category: Trp191 cationic radical]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:39:34 2008''

Revision as of 07:39, 2 July 2008

Image:1kok.png

Template:STRUCTURE 1kok

Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)

Template:ABSTRACT PUBMED 12237229

About this Structure

1KOK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases., Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL, J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:12237229

Page seeded by OCA on Wed Jul 2 10:39:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kok"
Personal tools